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- W2381766298 abstract "The effects of some protein modification reagents on the antivity of the malaotetraose-forming amylase have been studied. The enzyme was not affected by IAA, GEM, EDC and NAI modification, suggesting that thiol groups, carboxyl groups and tyosyl residues were non-essential to enzyme activity. The enzyme activity was remarkably decreased after DEP, NBS, HNBB modification. The results indicated that histidyl and tryptophyl residues seemed to be essential to the catolytic activity of the maltotetrose-forming amylase." @default.
- W2381766298 created "2016-06-24" @default.
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- W2381766298 date "1995-01-01" @default.
- W2381766298 modified "2023-09-25" @default.
- W2381766298 title "Chemical Modifocation of Maltotetroseforming Amylase from Alcaligenes sp" @default.
- W2381766298 hasPublicationYear "1995" @default.
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